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Database: UniProt
Entry: F7IHV2_CALJA
LinkDB: F7IHV2_CALJA
Original site: F7IHV2_CALJA 
ID   F7IHV2_CALJA            Unreviewed;      2252 AA.
AC   F7IHV2;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-SEP-2017, entry version 38.
DE   RecName: Full=Voltage-dependent R-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1E {ECO:0000313|Ensembl:ENSCJAP00000008406};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000008406, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000008406, ECO:0000313|Proteomes:UP000008225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000008406}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the
CC       entry of calcium ions into excitable cells and are also involved
CC       in a variety of calcium-dependent processes, including muscle
CC       contraction, hormone or neurotransmitter release, gene expression,
CC       cell motility, cell division and cell death. The isoform alpha-1E
CC       gives rise to R-type calcium currents. R-type calcium channels
CC       belong to the 'high-voltage activated' (HVA) group and are blocked
CC       by nickel, and partially by omega-agatoxin-IIIA (omega-Aga-IIIA).
CC       They are however insensitive to dihydropyridines (DHP), omega-
CC       conotoxin-GVIA (omega-CTx-GVIA), and omega-agatoxin-IVA (omega-
CC       Aga-IVA). Calcium channels containing alpha-1E subunit could be
CC       involved in the modulation of firing patterns of neurons which is
CC       important for information processing.
CC       {ECO:0000256|RuleBase:RU003808}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003808};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU003808}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family. {ECO:0000256|RuleBase:RU003808}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00448}.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSCJAP00000008406}.
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DR   EMBL; ACFV01050711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01050712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01050713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01050714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01050715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01050716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01050717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01050718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01050719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01050720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSCJAT00000008890; ENSCJAP00000008406; ENSCJAG00000004426.
DR   eggNOG; ENOG410INF5; Eukaryota.
DR   eggNOG; ENOG410YD06; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   Proteomes; UP000008225; Chromosome 18.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005449; VDCC_R_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF253; PTHR10037:SF253; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01633; RVDCCALPHA1.
DR   SMART; SM01062; Ca_chan_IQ; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|RuleBase:RU003808};
KW   Calcium channel {ECO:0000256|RuleBase:RU003808};
KW   Calcium transport {ECO:0000256|RuleBase:RU003808};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008225};
KW   Ion channel {ECO:0000256|RuleBase:RU003808};
KW   Ion transport {ECO:0000256|RuleBase:RU003808};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU003808};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003808}.
FT   TRANSMEM     93    110       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    130    150       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    162    180       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    221    243       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    295    316       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    328    350       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    477    497       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    503    521       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    603    625       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    680    703       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1133   1152       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1205   1223       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1271   1293       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1383   1408       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1464   1482       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1494   1517       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1523   1541       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1588   1606       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1681   1705       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1721   1756       EF-hand. {ECO:0000259|PROSITE:PS50222}.
FT   COILED      699    726       {ECO:0000256|SAM:Coils}.
FT   COILED     1080   1102       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2252 AA;  254911 MW;  F8138AE8C9EF9B5E CRC64;
     MARFGEAVVA RPGSGDGDSD QSRNRQGTPV PASGQAAAYK QTKAQRARTM ALYNPIPVRQ
     NCFTVNRSLF IFGEDNIVRK YAKKLIDWPP FEYMILATII ANCIVLALEQ HLPEDDKTPM
     SRRLEKTEPY FIGIFCFEAG IKIVALGFIF HKGSYLRNGW NVMDFIVVLS GILATAGTHF
     NTHVDLRTLR AVRVLRPLKL VSGIPSLQIV LKSIMKAMVP LLQIGLLLFF AILMFAIIGL
     EFYSGKLHRA CFMNNSGILE GFDPPHPCGV QGCPAGYECK DWIGPNDGIT QFDNILFAVL
     TVFQCITMEG WTTVLYNTND ALGATWNWLY FIPLIIIGSF FVLNLVLGVL SGEFAKERER
     VENRRAFMKL RRQQQIEREL NGYRAWIDKA EEVMLAEENK NAGTSALEVL RRATIKRSRT
     EAMTRDSSDE HCVDISSVGT PLARASIKST KVDGVSYFRH KERLLRISIR HMVKSQVFYW
     IVLSLVALNT ACVAIVHHNQ PQWLTHLLYY AEFLFLGLFL LEMSLKMYGM GPRLYFHSSF
     NCFDFGVTVG SIFEVVWAIF RPGTSFGISV LRALRLLRIF KITKYWASLR NLVVSLMSSM
     KSIISLLFLL FLFIVVFALL GMQLFGGRFN FNDGTPSANF DTFPAAIMTV FQILTGEDWN
     EVMYNGIRSQ GGVSSGMWSA IYFIVLTLFG NYTLLNVFLA IAVDNLANAQ ELTKDEQEEE
     EAFNQKHALQ KAKEVSPMSA PNMPSIERER RRRHHMSVWE QRTSQLRKHM QMSSQEALNR
     EEAPPMNPLN PLNPLSPLNP LNAHPSLYRR PRAIEGLALG LALEKFDEER ISRGGSLKGE
     GGDRSSTLDN QRTPLSLGQR ELPWLPRSCH GNCDPTQQEA GGGEAVVTFE DRARHRQSQR
     RSRHRRVRTE GKESSSASRS RSASQERSLD EAVPAEGEKE HELRGNHSAK EPTIQEERAQ
     DLRRTNSLML SRGSGLAGAL DEANTPLVLP HPELEVGKDA VLTEQEPEGS SEQALLGDVQ
     LDMGRVISHS EPDLSCITAN TDKAITESTS VTVAIPDVGP LVDSTVVHIS NKTDGEASPL
     KEAEIRDDEE EVENKKQKKE KRETGKAMVP HSSMFIFSTT NPIRRACHYI VNLRYFEMCI
     LLVIAASSIA LAAEDPVLTN SERNKVLRYF DYVFTGVFTF EMVIKMIDQG LILQDGSYFR
     DLWNILDFVV VVGALVAFAL AAFPRRTNKG RDIKTIKSLR VLRVLRPLKT IKRLPKLKAV
     FDCVVTSLKN VFNILIVYKL FMFIFAVIAV QLFKGKFFYC TDSSKDTEKE CIGNYVDHEK
     NKMEVKGREW KRHEFHYDNI IWALLTLFTV STGEGWPQVL QHSVDVTEED RGPSRSNRME
     MSIFYVVYFV VFPFFFVNIF VALIIITFQE QGDKMMEECS LEKNERACID FAISAKPLTR
     YMPQNRHTFQ YRVWHFVVSP SFEYTIMAMI ALNTVVLMMK YYSAPCTYEL ALKYLNIAFT
     MVFSLECVLK VIAFGFLNYF RDTWNIFDFI TVIGSITEII LTDSKLVNTS GFNMSFLKLF
     RAARLIKLLR QGYTIRILLW TFVQSFKALP YVCLLIAMLF FIYAIIGMQV FGNIKLDEES
     HINRHNNFRS FFGSLMLLFR SATGEAWQEI MLSCLGEKGC EPDTTAPSGQ NENERCGTDL
     AYVYFVSFIF FCSFLMLNLF VAVIMDNFEY LTRDSSILGP HHLDEFVRVW AEYDRAACGR
     IHYTEMYEML TLMSPPLGLG KRCPSKVAYK RLVLMNMPVA EDMTVHFTST LMALIRTALD
     IKIAKGGADR QQLDSELQKE TLAIWPHLSQ KMLDLLVPMP KASDLTVGKI YAAMMIMDYY
     KQSKVKKQRQ QLEEQKNAPM FQRMEPSSLP QEIIANAKAL PYLQQEHVSG LSGRTGYPSM
     SPLSPQEIFQ LACMDPADDG QFQEQQSLVV TDPSSMRRSF STIRDKRSNS SWLEEFSMER
     SSENTYKSRR RSYHSSLRLS AHRLNSDSGH KSDTHRSGGR ERGRSKERKH LLSPDVSRCN
     SEERGTQADW ESPERRQSRS PSEGRSQTPN QQGTGSLSES SIPSVSDTST PRRSRRQLPP
     VPPKPRPLLS YSSLIRHAGS ISPPADGSQE GSPLTSQALE SNNACLTESS NSPHPQQGQH
     ISPQRYISEP YLAQHEDSHA SDCGEEETLT FEAAVATSLG RSNTIGSAPP LRHSWQMPNG
     HYRRRRRGGP GSGMMCGAVN NLLSDTEEDD KC
//
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